Mechanism driving ß-arrestin translocation to the plasma membrane

Determine the cellular and molecular mechanism that drives the translocation of cytosolic ß-arrestins to the plasma membrane upon activation of seven transmembrane receptors (G protein–coupled receptors), beyond the established role of receptor phosphorylation in recruiting ß-arrestins.

Background

The authors show that ARIP inhibits agonist-induced ß-arrestin recruitment but does not recruit ß-arrestins on its own and does not alter G protein signaling. They infer that ARIP likely binds arrestins at the plasma membrane once migration has been initiated by receptor activation.

Despite extensive knowledge that receptor phosphorylation is essential for arrestin recruitment, the upstream process causing arrestins to leave the cytosol and move to the membrane is not defined, limiting mechanistic understanding of ARIP’s mode of action and arrestin dynamics.